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Database: UniProt
Entry: V9E2A2_PHYPR
LinkDB: V9E2A2_PHYPR
Original site: V9E2A2_PHYPR 
ID   V9E2A2_PHYPR            Unreviewed;       803 AA.
AC   V9E2A2;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=F443_20560 {ECO:0000313|EMBL:ETI32678.1};
OS   Phytophthora parasitica P1569.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI32678.1, ECO:0000313|Proteomes:UP000018721};
RN   [1] {ECO:0000313|EMBL:ETI32678.1, ECO:0000313|Proteomes:UP000018721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1569 {ECO:0000313|EMBL:ETI32678.1,
RC   ECO:0000313|Proteomes:UP000018721};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P1569.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00000448};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETI32678.1}.
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DR   EMBL; ANIZ01003593; ETI32678.1; -; Genomic_DNA.
DR   EMBL; ANIZ01003593; ETI32679.1; -; Genomic_DNA.
DR   AlphaFoldDB; V9E2A2; -.
DR   EnsemblProtists; ETI32678; ETI32678; F443_20560.
DR   EnsemblProtists; ETI32679; ETI32679; F443_20560.
DR   eggNOG; ENOG502QQ55; Eukaryota.
DR   OrthoDB; 5485475at2759; -.
DR   Proteomes; UP000018721; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018721};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..803
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015102181"
FT   DOMAIN          680..754
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   803 AA;  88340 MW;  24B35E54CA2B8724 CRC64;
     MLKSWFAAVL CTALGLAAQQ GTPLVSADQW DERADAIVAT FTDDDIIGQM TQIDINQLLT
     EDNKVDDDKV RAYAKMRVGS YLTSPFNNGP VNGTYMWTAD EWREVITRIQ EITMEENGGH
     PMVYGVDSVH GAIFVKDAVL FGQQINGGAS FNPDLVYEQG RITGRDTEAS GVPWVFGPIL
     GISRNPLWAR TFETFSEDPH INSVMGDAII RGLQSNNHTA ACMKHWIVYP KTPSGHDKDA
     VTVSDYDMMN YFFPPFKAAV DAGVISTMEN YISINGVPTV SNAKLMNALL RDDLGFDGMM
     VTDYAEINQL TDFHRTARNE TEATRISLTR ASVDMSMVAQ DTSFYNGTKA LLEQSPQFRE
     RLRESARRVV KMKLKLGLYE TPVPGEENLA LIGNDDDISA ALELARESIV LLQNNDSTLP
     IKEDASVFLT GFTADNIGRM CGGWTIAWQG YSDQDHLLTK GITVKSAMET LVGNDSFSFF
     NGLHPNGSYT EADLATAKEL ASKAEYTIAV IGEDTYAEKP GDIDDLALPA GQIEYVKELA
     STGTKVILVL FEGHPRLLGD LPENVHAVVN GLLACELGGQ AMAEIIYGKV NPSGRMPITY
     PKDQANIQMT YNHPVTSMCQ TQESDGAYYC ENQWDFGAGL SYTEFTYSEV RLSRNVVTSS
     AEDVVVSVDV TNSGSVAGKE TVMLFLIQPY NSLNVPEMKQ LKKFSKISLE PGQTQNVNFT
     LTADDWSVYY PQVGHGLKKV AEDCDYVVAI KPETDCDVYN ETAVANPLCA TFSLNTGEYP
     FGTFEEPCAL LQLVDLRGPK RMS
//
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